Information on EC 3.4.21.120 - oviductin

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The expected taxonomic range for this enzyme is: Tetrapoda

EC NUMBER
COMMENTARY hide
3.4.21.120
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RECOMMENDED NAME
GeneOntology No.
oviductin
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
preferential cleavage at Gly-Ser-Arg373-/- of glycoprotein gp43 in Xenopus laevis coelemic egg envelope to yield gp41
show the reaction diagram
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-
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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Uniprot
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
gene Ovch2
UniProt
Manually annotated by BRENDA team
female ICR
-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
55 kDa glycoprotein + H2O
?
show the reaction diagram
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the oviductal protease selectively hydrolyzes in vitro the 84 kDa and the 55 kDa glycoproteins of the coelomic envelope
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-
?
84 kDa glycoprotein + H2O
?
show the reaction diagram
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the oviductal protease selectively hydrolyzes in vitro the 84 kDa and the 55 kDa glycoproteins of the coelomic envelope
-
-
?
gp43 + H2O
gp41 + ?
show the reaction diagram
Nalpha-tert-butoxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Leu-Ser-Thr-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
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14% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Nalpha-tert-butoxycarbonyl-Leu-Thr-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Leu-Thr-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
12% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide + H2O
Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
-
-
-
?
Pro-Phe-Arg-4-methylcoumarin-7-amide + H2O
Pro-Phe-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
9% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
Pyr-Gly-Arg-4-methylcoumarin-7-amide + H2O
Pyr-Gly-Arg + 7-amino-4-methylcoumarin
show the reaction diagram
-
9% of the activity with Nalpha-tert-butoxycarbonyl-Phe-Ser-Arg-4-methylcoumarin-7-amide
-
-
?
additional information
?
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it is proposed that hamster oviductin is a mucin-type glycoprotein which might act as a protective secretion influencing the first steps of the reproductive process necessary for the normal triggering of fertilization and early embryonic development
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
gp43 + H2O
gp41 + ?
show the reaction diagram
additional information
?
-
-
it is proposed that hamster oviductin is a mucin-type glycoprotein which might act as a protective secretion influencing the first steps of the reproductive process necessary for the normal triggering of fertilization and early embryonic development
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-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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38% stimulation at 10 mM. 11% stimulation at 100 mM
KCl
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maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
LiCl
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maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaCl
-
maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaF
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maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
NaNO3
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maximal activity in 200-400 mM solution of monovalent salts is 200% of that in absence of added salt
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
antipain
-
0.05 mM, 35% inhibition
Aprotinin
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0.05 mM, 97% inhibition
diisopropyl fluorophosphate
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0.05 mM, 37% inhibition. Rapid and irreverible
EDTA
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0.05 mM, 90% inhibition
EGTA
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0.05 mM, 94% inhibition
guanidine hydrochloride
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competitive
leupeptin
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0.05 mM, 55% inhibition
p-aminobenzamidine
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competitive
Soybean trypsin inhibitor
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0.0025 mM, 84% inhibition
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additional information
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no inhibition by iodoacetamide, E-64, pepstatin or 1,10-phenanthroline
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.058
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-4-methylcoumarin-7-amide
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.8
Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-4-methylcoumarin-7-amide
Xenopus laevis
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0075
guanidine hydrochloride
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0.0041
p-aminobenzamidine
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
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Nalpha-tert-butoxycarbonylphenylalanylserylarginyl-4-methylcoumarin-7-amide
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
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more than 90% of maximal activity at pH 7.5 and at pH 8.5, less than 30% of maximal activity below pH 6.5
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
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and 8.0
8
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and 4.5
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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endocytic compartments in the blastomeres of developing embryos
Manually annotated by BRENDA team
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expressed in the chicken egg citelline membrane: using high-throughput, high-end LC-mass spectroscopy 137 proteins are identified. Specific components of the vitelline membrane not identified previously in other egg compartments include eight zona pellucida proteins, oviductin protease, and two ATPases
Manually annotated by BRENDA team
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endocytic compartments in the blastomeres of developing embryos
Manually annotated by BRENDA team
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negligible expression during the first three months of postnatal cervical differentiation. Transcripts are minimally detectable in the cervives of 4-month-old juveniles. Strong expression in the endocervices of adults is eliminated by ovariectomy and restored by estrogen treatment
Manually annotated by BRENDA team
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luminal epithelial cells of uterus
Manually annotated by BRENDA team
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immortalized human oviductal epithelial cell line
Manually annotated by BRENDA team
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after its release into the lumen of the oviduct, oviductin becomes associated with the zona pellucida of post-ovulatory oocytes. In unfertilized oocytes, oviductin is also detected in membrane invaginations along the oolemma and in some vesicles within multivesicular bodies
Manually annotated by BRENDA team
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it is speculated that receptors for hamster oviductin-1 are present at the apical cell surface of endometrial cells and that implantation of the developing blastocyst into the uterine wall is possible only following downregulation of these receptors
Manually annotated by BRENDA team
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oviductin is detected over the microvilli and within multivesicular bodies
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
of the non-ciliated oviduct cells
Manually annotated by BRENDA team
translational products stored in the pars recta granules need to be processed to become a proteolytically active 66000 Da form
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Manually annotated by BRENDA team
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of uterine epithelial cells
Manually annotated by BRENDA team
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of uterine epithelial cells
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
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x * 66000, SDS-PAGE under both nonreducing and reducing conditions
97000
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SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 66000, SDS-PAGE under both nonreducing and reducing conditions
additional information
oviductin is a multi-domain protein with a protease domain at the N-terminal region followed by two CUB domains and toward the C-terminal region another protease domain, which lacks an active histidine site, and one CUB domain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
relatively stable to rapid freezing in the presence of 20% glycerol. 90% of the activity remains after each freeze-thaw cycle
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene OVCH2, DNA and amino acid sequence determination and analysis
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